ChemInform Abstract: Acylase I Catalyzed Hydrolysis of para-Substituted (S)-Phenylalanine Derivatives from Mixtures of the Racemic ortho- and para-Substituted Isomers.

ChemInform ◽  
2010 ◽  
Vol 29 (41) ◽  
pp. no-no
Author(s):  
C. J. EASTON ◽  
J. B. HARPER
Keyword(s):  
2001 ◽  
Vol 66 (9) ◽  
pp. 1428-1433 ◽  
Author(s):  
J. Baxter ◽  
Y. Kim ◽  
M. Snowden
Keyword(s):  

1965 ◽  
Vol 13 (2) ◽  
pp. 117-124 ◽  
Author(s):  
V. K. HOPSU ◽  
R. S. SANTTI ◽  
G. G. GLENNER

Enzymes in guinea pig homogenates hydrolyzing a variety of halogenated and nonhalogenated acyl α- and β-naphthylamide substrates can be separated into two major groups on the basis of substrate hydrolysis rates, solubility and affector characteristics. Both groups of enzymes, those acting on the non-, mono- and dihalogenated acyl naphthylamides and those acting on trihalogen derivatives, have characteristics like those of arylesterases and are inseparable from enzymes hydrolyzing naphthol AS acetate. These enzymes are, However, separable on fractionation by starch gel electrophoresis and DEAE-cellulose chromatography from several enzymes catalyzing the hydrolysis of N-acyl amino acids (acylase I and II) and several amino acid β-naphthylamides. Species differences exist in the characteristics of enzymic hydrolysis of these acylarylamides.


Author(s):  
R. J. Barrnett ◽  
J. A. Higgins

The main products of intestinal hydrolysis of dietary triglycerides are free fatty acids and monoglycerides. These form micelles from which the lipids are absorbed across the mucosal cell brush border. Biochemical studies have indicated that intestinal mucosal cells possess a triglyceride synthesising system, which uses monoglyceride directly as an acylacceptor as well as the system found in other tissues in which alphaglycerophosphate is the acylacceptor. The former pathway is used preferentially for the resynthesis of triglyceride from absorbed lipid, while the latter is used mainly for phospholipid synthesis. Both lipids are incorporated into chylomicrons. Morphological studies have shown that during fat absorption there is an initial appearance of fat droplets within the cisternae of the smooth endoplasmic reticulum and that these subsequently accumulate in the golgi elements from which they are released at the lateral borders of the cell as chylomicrons.We have recently developed several methods for the fine structural localization of acyltransferases dependent on the precipitation, in an electron dense form, of CoA released during the transfer of the acyl group to an acceptor, and have now applied these methods to a study of the fine structural localization of the enzymes involved in chylomicron lipid biosynthesis. These methods are based on the reduction of ferricyanide ions by the free SH group of CoA.


Author(s):  
T. Baird ◽  
J.R. Fryer ◽  
S.T. Galbraith

Introduction Previously we had suggested (l) that the striations observed in the pod shaped crystals of β FeOOH were an artefact of imaging in the electron microscope. Contrary to this adsorption measurements on bulk material had indicated the presence of some porosity and Gallagher (2) had proposed a model structure - based on the hollandite structure - showing the hollandite rods forming the sides of 30Å pores running the length of the crystal. Low resolution electron microscopy by Watson (3) on sectioned crystals embedded in methylmethacrylate had tended to support the existence of such pores.We have applied modern high resolution techniques to the bulk crystals and thin sections of them without confirming these earlier postulatesExperimental β FeOOH was prepared by room temperature hydrolysis of 0.01M solutions of FeCl3.6H2O, The precipitate was washed, dried in air, and embedded in Scandiplast resin. The sections were out on an LKB III Ultramicrotome to a thickness of about 500Å.


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